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Conserved domains on  [gi|2318961066|gb|UYJ17973|]
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MAG: hypothetical protein OGM58_00210 [Veillonellaceae bacterium]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

LbetaH (left-handed parallel beta-helix) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 1-76 3.49e-33

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


The actual alignment was detected with superfamily member cd03357:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 169  Bit Score: 111.75  E-value: 3.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318961066   1 MISPDASILTVNHDFE----NTWIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVI 76
Cdd:cd03357    90 LIGPNVQIYTAGHPLDpeerNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 1-76 3.49e-33

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 111.75  E-value: 3.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318961066   1 MISPDASILTVNHDFE----NTWIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVI 76
Cdd:cd03357    90 LIGPNVQIYTAGHPLDpeerNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1-79 3.07e-32

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 108.42  E-value: 3.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318961066   1 MISPDASILTVNHDFEN--TWIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKK 78
Cdd:COG0110    55 LIGPGVTILTGNHPIDDpaTFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRK 134


                  .
gi 2318961066  79 V 79
Cdd:COG0110   135 R 135
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 1-79 2.22e-24

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 89.87  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318961066   1 MISPDASILTVNHDFE----NTWIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVI 76
Cdd:PRK10092  101 MLAPGVHIYTATHPLDpvarNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARII 180


                  ...
gi 2318961066  77 KKV 79
Cdd:PRK10092  181 KKL 183
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 22-78 1.92e-21

phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 82.90  E-value: 1.92e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2318961066  22 KCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKK 78
Cdd:TIGR03308 105 RAKRVTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRR 161
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
25-54 1.63e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 32.69  E-value: 1.63e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 2318961066 25 PVRIKKKAWIGAKAIIMPGVTIGEGAVIGS 54
Cdd:pfam00132  1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 1-76 3.49e-33

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 111.75  E-value: 3.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318961066   1 MISPDASILTVNHDFE----NTWIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVI 76
Cdd:cd03357    90 LIGPNVQIYTAGHPLDpeerNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1-79 3.07e-32

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 108.42  E-value: 3.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318961066   1 MISPDASILTVNHDFEN--TWIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKK 78
Cdd:COG0110    55 LIGPGVTILTGNHPIDDpaTFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRK 134


                  .
gi 2318961066  79 V 79
Cdd:COG0110   135 R 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 1-76 5.89e-29

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 99.07  E-value: 5.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318961066   1 MISPDASILTVNHDFENT-----WIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARV 75
Cdd:cd04647    29 LIGPNVTIYDHNHDIDDPerpieQGVTSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKV 108


                  .
gi 2318961066  76 I 76
Cdd:cd04647   109 I 109
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 24-78 1.54e-24

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 89.14  E-value: 1.54e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2318961066  24 KPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKK 78
Cdd:cd03349    72 GDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 1-79 2.22e-24

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 89.87  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318961066   1 MISPDASILTVNHDFE----NTWIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVI 76
Cdd:PRK10092  101 MLAPGVHIYTATHPLDpvarNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARII 180


                  ...
gi 2318961066  77 KKV 79
Cdd:PRK10092  181 KKL 183
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 22-77 7.28e-22

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 81.39  E-value: 7.28e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2318961066  22 KCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIK 77
Cdd:cd03358    64 ELKGTTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PRK10502 PRK10502
putative acyl transferase; Provisional
 2-77 1.14e-21

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 82.69  E-value: 1.14e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2318961066   2 ISPDASILTVNHDFEN-TWIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIK 77
Cdd:PRK10502  100 ISQKSYLCTGSHDYSDpHFDLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 22-78 1.92e-21

phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 82.90  E-value: 1.92e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2318961066  22 KCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKK 78
Cdd:TIGR03308 105 RAKRVTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRR 161
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 2-76 1.64e-20

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 77.65  E-value: 1.64e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2318961066   2 ISPDASILTVNHDFEN-TWIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVI 76
Cdd:cd05825    32 ISQGAYLCTGSHDYRSpAFPLITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 1-79 1.83e-18

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 75.04  E-value: 1.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318961066   1 MISPDASILT----VNHDFENTWIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVI 76
Cdd:PRK09527  103 LIAPNVTLSVtghpVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVI 182


                  ...
gi 2318961066  77 KKV 79
Cdd:PRK09527  183 REI 185
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 19-78 8.53e-17

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 70.67  E-value: 8.53e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2318961066  19 WIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKK 78
Cdd:PRK09677  124 RTLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKK 183
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 26-73 1.14e-15

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 67.52  E-value: 1.14e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2318961066  26 VRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPA 73
Cdd:TIGR03570 154 VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 26-72 1.50e-15

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 67.12  E-value: 1.50e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2318961066  26 VRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNP 72
Cdd:cd03360   151 VTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 33-80 1.94e-15

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 66.65  E-value: 1.94e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2318961066  33 WIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKKVG 80
Cdd:COG1045   125 VIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKG 172
PLN02357 PLN02357
serine acetyltransferase
 34-76 6.89e-12

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 58.74  E-value: 6.89e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2318961066  34 IGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVI 76
Cdd:PLN02357  287 IGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
PLN02694 PLN02694
serine O-acetyltransferase
 34-76 2.50e-11

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 56.96  E-value: 2.50e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2318961066  34 IGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVI 76
Cdd:PLN02694  221 IGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 27-79 7.06e-11

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 54.34  E-value: 7.06e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2318961066  27 RIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVT--KDVPDHTIAVGNPARVIKKV 79
Cdd:cd04645    79 TIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVREL 133
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 27-72 1.15e-10

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 52.44  E-value: 1.15e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2318961066  27 RIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNP 72
Cdd:cd03354    56 TIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-70 1.18e-10

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 55.50  E-value: 1.18e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2318961066   6 ASILTVNHDFENtwiiKCKPVrIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVG 70
Cdd:PRK14356  384 AGTITCNYDGVN----KHRTV-IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIA 443
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 34-79 1.22e-10

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 53.88  E-value: 1.22e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2318961066  34 IGAKAIIMPGVTIGEGAVIGSGAIVT--KDVPDHTIAVGNPARVIKKV 79
Cdd:COG0663    97 IGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVREL 144
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 13-73 3.59e-10

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 53.99  E-value: 3.59e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2318961066  13 HDFENTwIIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTK--DVPDHTIAVGNPA 73
Cdd:TIGR02353 634 HLFEDR-VMKSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
PLN02739 PLN02739
serine acetyltransferase
 27-79 5.58e-10

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 53.50  E-value: 5.58e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2318961066  27 RIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKKV 79
Cdd:PLN02739  259 KIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFV 311
cysE PRK11132
serine acetyltransferase; Provisional
 27-78 1.00e-09

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 52.39  E-value: 1.00e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2318961066  27 RIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKK 78
Cdd:PRK11132  195 KIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGK 246
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 27-77 2.16e-09

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 51.79  E-value: 2.16e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2318961066  27 RIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIK 77
Cdd:PRK14353  382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETK 432
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 27-79 2.25e-07

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 45.25  E-value: 2.25e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2318961066  27 RIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVT--KDVPDHTIAVGNPARVIKKV 79
Cdd:cd04650    80 KVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKL 134
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-78 4.58e-07

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 45.14  E-value: 4.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2318961066   6 ASILTVNHDFEntwiiKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKK 78
Cdd:PRK14357  369 AGTITCNYDGK-----KKNPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKE 436
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 27-79 5.63e-07

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 43.90  E-value: 5.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2318961066  27 RIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTK--DVPDHTIAVGNPARVIKKV 79
Cdd:cd04745    80 TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIREL 134
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 44-78 1.10e-06

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 43.86  E-value: 1.10e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2318961066  44 VTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKK 78
Cdd:COG1207   413 VTIGDGATIGAGSTITKDVPAGALAIARARQRNIE 447
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-78 1.12e-06

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 44.05  E-value: 1.12e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2318961066  10 TVNHDFENTWIIKckpvrIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKK 78
Cdd:PRK14354  383 TVNYDGKNKFKTI-----IGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIARARQVNKE 446
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 26-75 1.15e-06

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 43.85  E-value: 1.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2318961066  26 VRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARV 75
Cdd:COG1043   141 VEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARL 190
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-78 2.88e-06

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 42.99  E-value: 2.88e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2318961066   6 ASILTVNHDFENTwiikcKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARVIKK 78
Cdd:PRK14360  376 AGTITANYDGVKK-----HRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIKE 443
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 26-75 3.08e-06

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 42.80  E-value: 3.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2318961066  26 VRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARV 75
Cdd:cd03351   139 VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 28-70 8.35e-06

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 41.25  E-value: 8.35e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2318961066  28 IKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVG 70
Cdd:cd03353   147 IGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIA 189
PRK10191 PRK10191
putative acyl transferase; Provisional
 34-75 1.58e-05

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 40.26  E-value: 1.58e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2318961066  34 IGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPARV 75
Cdd:PRK10191  101 LGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 26-74 2.17e-05

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 40.08  E-value: 2.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2318961066  26 VRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAVGNPAR 74
Cdd:cd03352   151 TTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
PLN02296 PLN02296
carbonate dehydratase
 28-79 2.39e-05

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 40.11  E-value: 2.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2318961066  28 IKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKD--VPDHTIAVGNPARVIKKV 79
Cdd:PLN02296  139 VEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKL 192
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
34-75 7.65e-05

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 38.93  E-value: 7.65e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2318961066  34 IGAKAIIMPG------VTIGEGAVIGSGAIVTKDVPDHTIAVGNPARV 75
Cdd:PRK05289  144 VGDYAIIGGLtavhqfVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARL 191
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-76 1.39e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 37.99  E-value: 1.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2318961066   6 ASILTVNHDFENtwiiKCKPVrIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAV-GNPARVI 76
Cdd:PRK14352  385 ASSVFVNYDGVN----KHRTT-IGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVsEGPQRNI 451
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 26-62 1.45e-04

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 38.07  E-value: 1.45e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2318961066  26 VRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDV 62
Cdd:COG1044   109 AKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGV 145
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 24-63 1.71e-04

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 37.36  E-value: 1.71e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2318961066  24 KPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVP 63
Cdd:cd03350    74 TPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTP 113
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 26-62 2.23e-04

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 37.39  E-value: 2.23e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2318961066  26 VRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDV 62
Cdd:cd03352     2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGV 38
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 25-60 4.03e-04

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 36.63  E-value: 4.03e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2318961066  25 PVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTK 60
Cdd:COG2171   170 PVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTA 205
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 26-62 4.15e-04

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 36.59  E-value: 4.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2318961066  26 VRIKKKAWIgAKAIIMPGVTIGEGAVIgSGAIVTKDV 62
Cdd:COG0448   310 VRVESGAVV-ENSVIMPGVVIGEGAVI-ENAIIDKNV 344
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 25-63 4.40e-04

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 36.71  E-value: 4.40e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2318961066  25 PVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVP 63
Cdd:PRK11830  176 PVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTK 214
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 1-59 4.53e-04

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 34.92  E-value: 4.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 2318961066  1 MISPDASILTVNHDFENtwiikcKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVT 59
Cdd:cd00208   26 NIGPGAVIGAATGPNEK------NPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 14-73 5.14e-04

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 36.65  E-value: 5.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2318961066  14 DFENTW----IIKCKPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKD--VPDHTIAVGNPA 73
Cdd:TIGR02353 145 MLLGYRaergRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGqsIPDGERWHGSPA 210
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 28-58 9.16e-04

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 35.89  E-value: 9.16e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2318961066  28 IKKKAWIGAKAIIMPGVTIGEGAVIGSGAIV 58
Cdd:PRK00892  109 IDPSAKIGEGVSIGPNAVIGAGVVIGDGVVI 139
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-64 9.18e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 35.77  E-value: 9.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2318961066   6 ASILTVNHDFENtwiiKCKPVrIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPD 64
Cdd:PRK09451  380 AGTITCNYDGAN----KFKTI-IGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAE 433
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 26-67 1.09e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 35.57  E-value: 1.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2318961066  26 VRIKKKAWIgAKAIIMPGVTIGEGAVIgSGAIVTKDV--PDHTI 67
Cdd:PRK00844  338 VVVESGAEV-EDSVLMDGVRIGRGAVV-RRAILDKNVvvPPGAT 379
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 26-62 1.10e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 35.50  E-value: 1.10e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2318961066  26 VRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDV 62
Cdd:PRK00892  113 AKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV 149
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 28-57 1.20e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 35.38  E-value: 1.20e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2318961066  28 IKKKAWIGAKAIIMPGVTIGEGAVIGSGAI 57
Cdd:COG1044   123 IGAGVVIGDGVVIGPGVVIGDGVVIGDDCV 152
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
25-54 1.63e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 32.69  E-value: 1.63e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 2318961066 25 PVRIKKKAWIGAKAIIMPGVTIGEGAVIGS 54
Cdd:pfam00132  1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 26-58 3.29e-03

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 33.92  E-value: 3.29e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2318961066  26 VRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIV 58
Cdd:cd03352    14 AVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVI 46
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 28-79 4.38e-03

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 33.63  E-value: 4.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2318961066  28 IKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVT---KDVPDHTIaVGNPARVIKKV 79
Cdd:PRK13627   91 IGRDALVGMNSVIMDGAVIGEESIVAAMSFVKagfQGEKRQLL-MGTPARAVRSV 144
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 26-69 4.53e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 33.69  E-value: 4.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2318961066  26 VRIKKKAWIgAKAIIMPGVTIGEG-----AVIGSGAIVTKDV----PDHTIAV 69
Cdd:PRK05293  315 VQVGEGSVV-KDSVIMPGAKIGENvvierAIIGENAVIGDGViiggGKEVITV 366
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 32-58 4.69e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 33.84  E-value: 4.69e-03
                          10        20
                  ....*....|....*....|....*..
gi 2318961066  32 AWIGAKAIIMPGVTIGEGAVIGSGAIV 58
Cdd:COG1044   103 AVIDPSAKIGEGVSIGPFAVIGAGVVI 129
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 28-62 4.76e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 33.57  E-value: 4.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2318961066  28 IKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDV 62
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGV 137
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 24-62 5.56e-03

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 33.54  E-value: 5.56e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2318961066  24 KPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDV 62
Cdd:cd03352    18 EGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGC 56
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 24-76 8.04e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 33.07  E-value: 8.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2318961066  24 KPVRIKKKAWIGAKAIIMPGVTIGEGAVIGSGAIVTKDVPDHTIAvGNPARVI 76
Cdd:PRK12461   28 ANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEPQDFTYK-GEESRLE 79
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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